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1 e modified by variation in the gene encoding catechol O-methyltransferase.
2 thionine ([3H]SAM) in presence of endogenous catechol-O-methyltransferase.
3 od substrates for recombinant and endogenous catechol-O-methyltransferase.
4 hylation of select tyrphostins by endogenous catechol-O-methyltransferase.
5 In genetically modified mice with reduced catechol-O-methyltransferase activity there was selectiv
7 ethylated to less polar monomethyl ethers by catechol-O-methyltransferase, an enzyme present in many
8 ently reported isotope-effect variations for catechol-O-methyltransferase and its mutant structures.
10 receptor, ATP-binding cassette subfamily B, catechol-O-methyltransferase, and cytochrome 2D6 current
11 mechanism of inhibition by quercetin of the catechol O-methyltransferase-catalyzed O-methylation of
13 allele encoding the low activity variant of catechol O-methyltransferase (COMT) and aggressive behav
17 ional polymorphism (Val(108/158) Met) in the catechol O-methyltransferase (COMT) gene and eye trackin
18 etween the Val158/108Met polymorphism of the catechol O-methyltransferase (COMT) gene and schizophren
19 tional polymorphism (val(158)met) within the catechol O-methyltransferase (COMT) gene underlies some
20 could result from haploinsufficiency of the catechol O-methyltransferase (COMT) gene, located within
31 in Parkinson's disease, namely the genes for catechol-O-methyltransferase (COMT Val(158)Met) and micr
33 ltransferase activity, the methyltransferase catechol-O-methyltransferase (COMT) and a known selectiv
34 ies of genetic variation in these systems in catechol-O-methyltransferase (COMT) and in metabotropic
35 he genotype of the Val158Met polymorphism in catechol-O-methyltransferase (COMT) as an index of relat
40 i) to determine whether polymorphisms in the catechol-O-methyltransferase (COMT) gene affect the rela
42 methionine (Val(158)Met) polymorphism in the catechol-O-methyltransferase (COMT) gene has been associ
43 ect of the Val108/158Met polymorphism in the catechol-O-methyltransferase (COMT) gene in children bef
45 functional polymorphism (Val(158)Met) in the catechol-O-methyltransferase (COMT) gene is associated w
49 ional polymorphism (Val(108/158) Met) in the catechol-O-methyltransferase (COMT) gene, which accounts
50 a functional polymorphism (Val158Met) in the catechol-O-methyltransferase (COMT) gene, whose protein
51 r (OPRM1), multidrug resistance (ABCB1), and catechol-o-methyltransferase (COMT) genes are associated
53 or placebo (n = 537) and were stratified by catechol-O-methyltransferase (COMT) genotype activity (h
54 A functional polymorphism in the gene for catechol-O-methyltransferase (COMT) has been shown to af
68 human TR3 gene overlapped with the gene for catechol-O-methyltransferase (COMT) on a complementary D
71 uals homozygous for the met158 allele of the catechol-O-methyltransferase (COMT) polymorphism (val158
73 our-hour urinary hydroxytyrosol and HVAL and catechol-O-methyltransferase (COMT) rs4680 genotypes wer
74 Here we show that pregnant mice deficient in catechol-O-methyltransferase (COMT) show a pre-eclampsia
75 as a function of baseline PFC DA [indexed by catechol-O-methyltransferase (COMT) Val(158)Met genotype
76 cortex plasticity, while additionally taking catechol-O-methyltransferase (COMT) Val158Met and kidney
78 authors assessed the association between the catechol-O-methyltransferase (COMT) Val158Met polymorphi
79 t study, we address the role of the gene for catechol-O-methyltransferase (COMT), a key modulator of
80 els are associated with genetic variation in catechol-O-methyltransferase (COMT), a regulatory enzyme
81 oratory has identified an early reduction in catechol-O-methyltransferase (COMT), an enzyme responsib
83 he DAT1 VNTR and functional polymorphisms in catechol-O-methyltransferase (COMT), DRD2, and DRD4 were
85 metabolite of estradiol and is generated by catechol-o-methyltransferase (COMT), induces invasion of
87 in inactivating and packaging NE, including catechol-O-methyltransferase (COMT), monoamine oxidase-A
88 is amplified by allelic variants in a gene, catechol-O-methyltransferase (COMT), regulating catechol
89 (OPRD1), cannabinoid receptor 1 (CNR1), and catechol-o-methyltransferase (COMT), was strongly associ
90 enols are very rapidly O-methylated by human catechol-O-methyltransferase (COMT), we are interested i
91 ion of a fungal tyrosinase and the mammalian catechol-O-methyltransferase (COMT), which can effect th
92 he enzymes proline dehydrogenase (PRODH) and catechol-O-methyltransferase (COMT), which modulate the
93 s and quercetin strongly inhibit human liver catechol-O-methyltransferase (COMT)-mediated O-methylati
99 ith a functional polymorphism (Val158Met) in catechol-O-methyltransferase [COMT], a gene that indexes
101 gle gene regions (e.g. opioid receptor mu-1, catechol-O-methyltransferase, cytochrome P450 2D6) and o
102 y of properties is observed between GNMT and catechol O-methyltransferase, despite significant differ
103 unctional polymorphism (val(158)-met) in the catechol O-methyltransferase gene, which has been shown
104 enotype at the Val158Met polymorphism of the catechol-O-methyltransferase gene predicts both impulsiv
108 le nucleotide tandem repeat, and the Val/Val catechol-O-methyltransferase genotype had greater decrea
110 a proof-of-concept, we study three enzymes (catechol-O-methyltransferase, glucose-6-phosphate dehydr
111 hydroxyestradiol by hamster kidney cytosolic catechol O-methyltransferase (IC50 approximately 10-14 m
112 in which we administered the brain penetrant catechol-O-methyltransferase inhibitor tolcapone or plac
114 g several other medications, such as MAOBIs, catechol-O-methyltransferase inhibitors, or dopamine ago
115 ibution of ER proteins, such as calnexin and catechol-O-methyltransferase, into a large centrosomal a
116 te to changes in cortical dopamine levels as catechol-O-methyltransferase is the main mode of inactiv
117 22q11.2 deletion syndrome, we identified the catechol-O-methyltransferase low-activity allele (COMT(L
118 the differential activity of membrane-bound catechol-O-methyltransferase (MB-COMT) due to altered pr
119 enosyl-L-homocysteine, a potent inhibitor of catechol-O-methyltransferase-mediated methylation of 3,4
120 oncompetitive inhibitor of DNMTs) during the catechol-O-methyltransferase-mediated O-methylation of t
122 10 homozygous for Val/Val and 10 for Met/Met catechol-O-methyltransferase polymorphisms) underwent (1
123 e-derivatives like 3-iodothyronamine (T1AM), catechol-O-methyltransferase products like 3-methoxytyra
124 A common polymorphism in the human gene for catechol-O-methyltransferase results in replacement of V
125 r O-methylation by human recombinant soluble catechol-O-methyltransferase (S-COMT) is a feasible deto
126 aken together, we concluded that CTOMT1 is a catechol-O-methyltransferase that produces guaiacol in t
128 hic Parkinson's disease as a function of the catechol-O-methyltransferase Val(158)Met polymorphism us
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